ID   DPOL_VZVD               Reviewed;        1194 AA.
AC   P09252;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 123.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
DE            EC=3.1.26.4;
GN   ORFNames=ORF28;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC   Varicellovirus humanalpha3; Human herpesvirus 3.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
CC   -!- FUNCTION: Replicates viral genomic DNA. The replication complex is
CC       composed of six viral proteins: the DNA polymerase, processivity
CC       factor, primase, primase-associated factor, helicase, and ssDNA-binding
CC       protein. Additionally, the polymerase contains an intrinsic
CC       ribonuclease H (RNase H) activity that specifically degrades RNA/DNA
CC       heteroduplexes or duplex DNA substrates in the 5' to 3' direction.
CC       Therefore, it can catalyze the excision of the RNA primers that
CC       initiate the synthesis of Okazaki fragments at a replication fork
CC       during viral DNA replication (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.7;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC   -!- SUBUNIT: Forms a complex with the ssDNA-binding protein, the DNA
CC       polymerase processivity factor, and the alkaline exonuclease. Interacts
CC       with the helicase-primase complex composed of the primase, the helicase
CC       and the primase-associated factor; this interaction may coordinate
CC       leading and lagging strand DNA synthesis at the replication fork (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Note=the protein is
CC       present at discrete sites in nuclei, called replication compartments
CC       where viral DNA replication occurs. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; X04370; CAA27911.1; -; Genomic_DNA.
DR   PIR; B27214; DJBE28.
DR   AlphaFoldDB; P09252; -.
DR   SMR; P09252; -.
DR   BindingDB; P09252; -.
DR   ChEMBL; CHEMBL4859; -.
DR   DrugBank; DB00787; Acyclovir.
DR   DrugCentral; P09252; -.
DR   Proteomes; UP000002602; Segment.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   FunFam; 1.10.132.60:FF:000011; DNA polymerase catalytic subunit; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR050240; DNA_pol_type-B.
DR   InterPro; IPR061942; Herpes_Pol_N.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF31254; Herpes_Pol_N; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW   Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1194
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000046525"
SQ   SEQUENCE   1194 AA;  134048 MW;  C0D5F0EA8D0D81E0 CRC64;
     MAIRTGFCNP FLTQASGIKY NPRTGRGSNR EFLHSYKTTM SSFQFLAPKC LDEDVPMEER
     KGVHVGTLSR PPKVYCNGKE VPILDFRCSS PWPRRVNIWG EIDFRGDKFD PRFNTFHVYD
     IVETTEAASN GDVSRFATAT RPLGTVITLL GMSRCGKRVA VHVYGICQYF YINKAEVDTA
     CGIRSGSELS VLLAECLRSS MITQNDATLN GDKNAFHGTS FKSASPESFR VEVIERTDVY
     YYDTQPCAFY RVYSPSSKFT NYLCDNFHPE LKKYEGRVDA TTRFLMDNPG FVSFGWYQLK
     PGVDGERVRV RPASRQLTLS DVEIDCMSDN LQAIPNDDSW PDYKLLCFDI ECKSGGSNEL
     AFPDATHLED LVIQISCLLY SIPRQSLEHI LLFSLGSCDL PQRYVQEMKD AGLPEPTVLE
     FDSEFELLIA FMTLVKQYAP EFATGYNIVN FDWAFIMEKL NSIYSLKLDG YGSINRGGLF
     KIWDVGKSGF QRRSKVKING LISLDMYAIA TEKLKLSSYK LDSVAREALN ESKRDLPYKD
     IPGYYASGPN TRGIIGEYCI QDSALVGKLF FKYLPHLELS AVARLARITL TKAIYDGQQV
     RIYTCLLGLA SSRGFILPDG GYPATFEYKD VIPDVGDVEE EMDEDESVSP TGTSSGRNVG
     YKGARVFDPD TGFYIDPVVV LDFASLYPSI IQAHNLCFTT LTLNFETVKR LNPSDYATFT
     VGGKRLFFVR SNVRESLLGV LLKDWLAMRK AIRARIPGSS SDEAVLLDKQ QAAIKVVCNS
     VYGFTGVAQG FLPCLYVAAT VTTIGRQMLL STRDYIHNNW AAFERFITAF PDIESSVLSQ
     KAYEVKVIYG DTDSVFIRFK GVSVEGIAKI GEKMAHIIST ALFCPPIKLE CEKTFIKLLL
     ITKKKYIGVI YGGKVLMKGV DLVRKNNCQF INDYARKLVE LLLYDDTVSR AAAEASCVSI
     AEWNRRAMPS GMAGFGRIIA DAHRQITSPK LDINKFVMTA ELSRPPSAYI NRRLAHLTVY
     YKLVMRQGQI PNVRERIPYV IVAPTDEVEA DAKSVALLRG DPLQNTAGKR CGEAKRKLII
     SDLAEDPIHV TSHGLSLNID YYFSHLIGTA SVTFKALFGN DTKLTERLLK RFIPETRVVN
     VKMLNRLQAA GFVCIHAPCW DNKMNTEAEI TEEEQSHQIM RRVFCIPKAI LHQS
//